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Peterson D, Schön A, Söll D. The nucleotide sequences of barley cytoplasmic glutamate transfer RNAs and structural features essential for formation of δ-aminolevulinic acid. Plant Mol Biol. 1988;11(3):293-9doi: 10.1007/BF00027386.
Peterson, D., Schön, A., & Söll, D. (1988). The nucleotide sequences of barley cytoplasmic glutamate transfer RNAs and structural features essential for formation of δ-aminolevulinic acid. Plant molecular biology, 11(3), 293-9. https://doi.org/10.1007/BF00027386
Peterson, D, et al. "The nucleotide sequences of barley cytoplasmic glutamate transfer RNAs and structural features essential for formation of δ-aminolevulinic acid." Plant molecular biology vol. 11,3 (1988): 293-9. doi: https://doi.org/10.1007/BF00027386
Peterson D, Schön A, Söll D. The nucleotide sequences of barley cytoplasmic glutamate transfer RNAs and structural features essential for formation of δ-aminolevulinic acid. Plant Mol Biol. 1988 May;11(3):293-9. doi: 10.1007/BF00027386. PMID: 24272342.
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Plant Mol Biol. 1988 May;11(3):293-9. doi: 10.1007/BF00027386.

The nucleotide sequences of barley cytoplasmic glutamate transfer RNAs and structural features essential for formation of δ-aminolevulinic acid.

Plant molecular biology

D Peterson, A Schön, D Söll

Affiliations

  1. Department of Molecular Biophysics & Biochemistry, Yale University, P.O. Box 6666, 06511, New Haven, CT, USA.

PMID: 24272342 DOI: 10.1007/BF00027386

Abstract

In chloroplasts and a number of prokaryotes, δ-aminolevulinic acid (ALA), the universal precursor of porphyrins, is synthesized by a multistep enzymatic pathway with glutamyl-tRNA(Glu) as an intermediate. The ALA synthesizing system from barley chloroplasts is highly specific in its tRNA requirement for chloroplast tRNA(Glu); a number of other Glu-tRNAs are inactive in ALA formation although they can be glutamylated by chloroplast aminoacyl-tRNA synthetases. In order to obtain more information about the structural features defining the ability of a tRNA to be recognized by the ALA synthesizing enzymes, we purified and sequenced two cytoplasmic tRNA(Glu) species from barley embryos which are inactive in ALA synthesis. By using glutamylated tRNAs as a substrate for the overall reaction, we showed that Glu-tRNA reductase is the enzyme responsible for tRNA discrimination.

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